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UniProtKB/Swiss-Prot entry P31751


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AKT2_HUMAN
Primary accession number P31751
Secondary accession numbers Q0VAN1 Q68GC0
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on November 1, 1995 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 91)
Name and origin of the protein
Protein name RAC-beta serine/threonine-protein kinase
Synonyms EC 2.7.11.1
RAC-PK-beta
Protein kinase Akt-2
Protein kinase B, beta
PKB beta
Gene name
Name: AKT2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epithelium;
PubMed=1801921 [NCBI, ExPASy, EBI, Israel, Japan]
Jones P.F., Jakubowicz T., Hemmings B.A.;
"Molecular cloning of a second form of rac protein kinase.";
Cell Regul. 2:1001-1009(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1409633 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng J.Q., Godwin A.K., Bellacosa A., Taguchi T., Franke T.F., Hamilton T.C., Tsichlis P.N., Testa J.R.;
"AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas.";
Proc. Natl. Acad. Sci. U.S.A. 89:9267-9271(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-277.
Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[5]
CHARACTERIZATION, AND PHOSPHORYLATION AT THR-309 BY PDPK1.
PubMed=9512493 [NCBI, ExPASy, EBI, Israel, Japan]
Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.;
"Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha.";
Biochem. J. 331:299-308(1998).
[6]
INTERACTION WITH MTCP1; TCL1A AND TCL1B.
DOI=10.1016/S1097-2765(00)00039-3; PubMed=10983986 [NCBI, ExPASy, EBI, Israel, Japan]
Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.;
"The protooncogene TCL1 is an Akt kinase coactivator.";
Mol. Cell 6:395-407(2000).
[7]
MUTAGENESIS OF THR-309 AND SER-474, AND PHOSPHORYLATION AT THR-309 AND SER-474.
DOI=10.1016/j.bbagen.2005.04.002; PubMed=15890450 [NCBI, ExPASy, EBI, Israel, Japan]
Baer K., Lisinski I., Gompert M., Stuhlmann D., Schmolz K., Klein H.W., Al-Hasani H.;
"Activation of a GST-tagged AKT2/PKBbeta.";
Biochim. Biophys. Acta 1725:340-347(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
VARIANTS [LARGE SCALE ANALYSIS] VAL-188 AND LYS-208.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M77198; AAA36585.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M95936; AAA58364.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC120994; AAI20995.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY708392; AAT97984.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A46288; A46288.
RefSeq NP_001617.1; -.
UniGene Hs.631535
3D structure databases
PDB
1GZK; X-ray; 2.30 A; A=146-460.[ExPASy / RCSB / EBI]
1GZN; X-ray; 2.50 A; A=146-480.[ExPASy / RCSB / EBI]
1GZO; X-ray; 2.75 A; A=146-460.[ExPASy / RCSB / EBI]
1MRV; X-ray; 2.80 A; A=143-481.[ExPASy / RCSB / EBI]
1MRY; X-ray; 2.80 A; A=143-481.[ExPASy / RCSB / EBI]
1O6K; X-ray; 1.70 A; A=146-481.[ExPASy / RCSB / EBI]
1O6L; X-ray; 1.60 A; A=146-467.[ExPASy / RCSB / EBI]
1P6S; NMR; -; A=1-111.[ExPASy / RCSB / EBI]
2UW9; X-ray; 2.10 A; A=146-477.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GZK; -.
1GZN; -.
1GZO; -.
1MRV; -.
1MRY; -.
1O6K; -.
1O6L; -.
1P6S; -.
2UW9; -.
DisProt DP00304; -.
ModBase P31751.
Protein-protein interaction databases
IntAct P31751; -.
PTM databases
PhosphoSite P31751; -.
Enzyme and pathway databases
Reactome REACT_1123; Inhibition of HSL.
REACT_498; Signaling by insulin receptor.
Polymorphism databases
NIEHS-SNPs AKT2.
Organism-specific databases
H-InvDB HIX0015131; -.
HGNC HGNC:392; AKT2.
GenAtlas AKT2.
HPA CAB004204; -.
MIM 164731; gene. [NCBI / EBI]
PharmGKB PA24685; -.
GeneCards P31751.
Gene expression databases
ArrayExpress P31751; -.
CleanEx HS_AKT2; -.
GermOnline ENSG00000105221; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004674; Molecular function: protein serine/threonine kinase activity (traceable author statement from ProtInc).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR015744; Akt.
IPR001849; PH.
IPR011993; PH_type.
IPR000961; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
PANTHER PTHR22985:SF69; Akt; 1.
Pfam PF00169; PH; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00233; PH; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS50003; PH_DOMAIN; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P31751.
Genome annotation databases
Ensembl ENSG00000105221; Homo sapiens. [Contig view]
GeneID 208; -.
KEGG hsa:208; -.
Phylogenomic databases
HOGENOM P31751; -.
HOVERGEN P31751; -.
Other
BindingDB P31751; -.
LinkHub P31751; -.
NextBio 836; -.
SOURCE AKT2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   481  481     RAC-beta serine/threonine-protein kinase. PRO_0000085608
DOMAIN   5   108  104     PH. 
DOMAIN   152   409  258     Protein kinase. 
DOMAIN   410   481  72     AGC-kinase C-terminal. 
NP_BIND   158   166  9     ATP (By similarity). 
ACT_SITE   275   275        Proton acceptor (By similarity). 
BINDING   181   181        ATP (By similarity). 
MOD_RES   126   126        Phosphoserine. 
MOD_RES   309   309        Phosphothreonine; by PDPK1. 
MOD_RES   474   474        Phosphoserine. 
VARIANT   188   188  1     I -> V. VAR_040356 [3D]
VARIANT   208   208  1     R -> K. VAR_040357 [3D]
MUTAGEN   309   309        T->E: Constitutively active; when associated with D-474. 
MUTAGEN   474   474        S->D: Constitutively active; when associated with E-309. 
CONFLICT   478   481        SIRE -> FREEKDLLMSLFVSLILFSDFSSLKSHSFSSNFILLSF SSLKK (in Ref. 1; AAA36585). 
STRAND   6    15  10      
STRAND   17    20  4      
STRAND   22    30  9      
TURN   31    33  3      
STRAND   34    40  7      
STRAND   45    47  3      
STRAND   52    56  5      
STRAND   58    60  3      
STRAND   62    65  4      
STRAND   67    75  9      
STRAND   86    92  7      
HELIX   93   110  18      
HELIX   149   151  3      
STRAND   152   160  9      
STRAND   162   171  10      
TURN   172   174  3      
STRAND   177   184  8      
TURN   185   187  3      
TURN   199   202  4      
HELIX   203   206  4      
STRAND   215   220  6      
STRAND   222   230  9      
HELIX   237   242  6      
HELIX   249   268  20      
HELIX   278   280  3      
STRAND   281   283  3      
STRAND   289   291  3      
HELIX   319   324  6      
HELIX   330   345  16      
STRAND   351   353  3      
HELIX   358   364  7      
HELIX   375   384  10      
HELIX   389   391  3      
TURN   397   399  3      
HELIX   400   404  5      
HELIX   414   418  5      
Sequence information
Length: 481 AA [This is the length of the unprocessed precursor] Molecular weight: 55769 Da [This is the MW of the unprocessed precursor] CRC64: B18C87A7246BFB24 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP PLNNFSVAEC 

        70         80         90        100        110        120 
QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM RAIQMVANSL KQRAPGEDPM 

       130        140        150        160        170        180 
DYKCGSPSDS STTEEMEVAV SKARAKVTMN DFDYLKLLGK GTFGKVILVR EKATGRYYAM 

       190        200        210        220        230        240 
KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH 

       250        260        270        280        290        300 
LSRERVFTEE RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG 

       310        320        330        340        350        360 
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHERLFE 

       370        380        390        400        410        420 
LILMEEIRFP RTLSPEAKSL LAGLLKKDPK QRLGGGPSDA KEVMEHRFFL SINWQDVVQK 

       430        440        450        460        470        480 
KLLPPFKPQV TSEVDTRYFD DEFTAQSITI TPPDRYDSLG LLELDQRTHF PQFSYSASIR 


E 

P31751 in FASTA format

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